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| Product Name | DnaK, Recombinant, E. coli (HSP-70, HSP70, Dnak ATPase Binding Domain) |
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| Description | Purity ~95% (RP-HPLC, SDS-PAGE). DnaK, originally identified for its DNA replication by bacteriophage l in E. coli is the bacterial HSP-70 chaperone. This protein is involved in the folding and assembly of newly synthesized polypeptide chains and in preventing the aggregation of stress-denatured proteins. DnaK (aa1-384) is N-terminal ATPase domain and ATP bound to the ATPase domain induces a conformational change in the substrate binding domain (residues 385-638). The protein coding region of the ATPase domain of DNAK (aa1-384) was amplified by PCR and cloned into an E. coli expression vector. The ATPase domain of DNAK was purified to apparent homogeneity by using conventional column chromatography techniques. Source: Recombinant protein corresponding to a single, non-glycosylated polypeptide chain containing 384aa from DnaK Substrate Binding Domain, expressed in E. coli. Molecular Weight: ~48.1kD AA Sequence: MGKIIGIDLG TTNSCVAIMD GTTPRVLENA EGDRTTPSII AYTQDGETLV GQPAKRQAVTNPQNTLFAIK |
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| Size | 20ug |
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| Concentration | n/a |
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| Applications | n/a |
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| Other Names | n/a |
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| Gene, Accession, CAS # | n/a |
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| Catalog # | 208852 |
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| Order / More Info | DnaK, Recombinant, E. coli (HSP-70, HSP70, Dnak ATPase Binding Domain) from UNITED STATES BIOLOGICAL |
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| Product Specific References | n/a |
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